Structural, Kinetic, and Calorimetric Characterization of the Cold-active Phosphoglycerate Kinase from the AntarcticPseudomonas sp. TACII18

Bentahir, Mostafa; Feller, Georges; Aittaleb, Mohamed; Lamotte‐Brasseur, Josette; Himri, Touhami; Chessa, Jean-Pierre; Gerday, Charles

doi:10.1074/jbc.275.15.11147

Cited by 94 publications

(85 citation statements)

References 43 publications

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“…A decrease in global stability may in turn provide the appropriate plasticity around the catalytic residues necessary to adapt the catalytic efficiency to low temperatures. However, as previously mentioned, the reduced stability related to the low stability of the psychrophilic enzyme may not necessarily arise from the general reduction in the strength of intramolecular forces, but from the weakened interactions in one or a few important regions of the structure (localized flexibility) (26,28,32,63). Lines of direct evidence of differences in stability between some domains and the entire structure have been provided by DSC studies (28,26).…”

Section: Oligomeric Enzymesmentioning

confidence: 96%

“…The lower stability of cold-active enzymes could also originate from weakened interactions in one or a few regions of the structure. Localized flexibility has been demonstrated by microcalorimetric studies of multidomain proteins (26)(27)(28). In psychrophilic chitobiase and the a-amylase precursor, differences in stability can be found between regions carrying the active site and the other moieties of the protein: The active site is embedded in a heatlabile domain, whereas the stability of other domains is unaffected or even enhanced.…”

Section: Psychrophilic Enzymesmentioning

confidence: 99%

“…mentarities with the substrate (28). Each protein uses one or a combination of possible structural adjustments to reduce the local or global stability of the molecular edifice.…”

Section: Psychrophilic Enzymesmentioning

confidence: 99%

“…However, as previously mentioned, the reduced stability related to the low stability of the psychrophilic enzyme may not necessarily arise from the general reduction in the strength of intramolecular forces, but from the weakened interactions in one or a few important regions of the structure (localized flexibility) (26,28,32,63). Lines of direct evidence of differences in stability between some domains and the entire structure have been provided by DSC studies (28,26). In these cases, cold-adapted enzymes contain some elements controlling protein stability and affinity for the substrate and other elements conferring the required flexibility for an efficient catalysis at the environmental temperature.…”

Section: Oligomeric Enzymesmentioning

confidence: 99%

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Extreme Catalysts from Low-Temperature Environments

et al. 2004

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Cold-loving or psychrophilic organisms are widely distributed in nature as a large part of the earth's surface is at temperatures around 0°C. To maintain metabolic rates and to prosper in cold environments, these extremophilic organisms have developed a vast array of adaptations. One main adaptive strategy developed in order to cope with the reduction of chemical reaction rates induced by low temperatures is the synthesis of cold-adapted or psychrophilic enzymes. These enzymes are characterized by a high catalytic activity at low temperatures associated with a low thermal stability. A study of protein adaptation strategies suggests that the high activity of psychrophilic enzymes could be achieved by the destabilization of the active site, allowing the catalytic center to be more flexible at low temperatures, whereas other protein regions may be destabilized or as rigid as their mesophilic counterparts. Due to these particular properties, psychrophilic enzymes offer a high potential not only for fundamental research but also for biotechnological applications.[Key words: psychrophile, extremophiles, cold adaptation, enzyme kinetics, flexibility strategy]Life under low-temperature conditions was identified as early as 1840 by Hooker, who observed that algae were associated with sea ice. In 1887, Forster was the first who reported that microorganisms isolated from fish could grow well at 0°C (1). The term "psychrophilic" was first used in 1902 by Schmidt-Nielsen to describe such cold-adapted organisms (2). Psychrophile is defined as an organism, prokaryotic or eukaryotic, living permanently at temperatures close to the freezing point of water in thermal equilibrium with the medium. Thus psychrophiles are numerous, including a large range of species of gram-positive and gram-negative bacteria, yeast, algae, marine invertebrates, insects and polar fish, and are widely distributed (3). Psychrophiles have developed mechanisms of adaptation to temperature including a huge range of structural and physiological adjustments in order to cope with the deleterious effect of low temperatures. Indeed, they display metabolic fluxes at low temperatures that are more or less comparable to those exhibited by closely related mesophiles living at moderate temperatures (4-6). This is explained by the capability of these psychrophilic organisms to produce "cold-adapted" enzymes which are able to cope with the reduction of chemical reaction rates induced by low temperatures. However, most cellular adaptations to low temperatures and the underlying molecular mechanisms are not fully understood and are still being investigated. Moreover, a study of proteins and enzymes from cold-adapted organisms is not only useful in the understanding of some general processes related to the protein structure and function but also in protein folding investigations. In addition, cold-active and heat-labile psychrophilic enzymes possess an interesting biotechnological potential.

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Section: Oligomeric Enzymesmentioning

confidence: 96%

Section: Psychrophilic Enzymesmentioning

confidence: 99%

“…mentarities with the substrate (28). Each protein uses one or a combination of possible structural adjustments to reduce the local or global stability of the molecular edifice.…”

Section: Psychrophilic Enzymesmentioning

confidence: 99%

Section: Oligomeric Enzymesmentioning

confidence: 99%

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Extreme Catalysts from Low-Temperature Environments

et al. 2004

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“…observed for salmon trypsin [21], subtilisin from the Antarctic Bacillus TA39 [22], lactate dehydrogenase from Antarctic notothenoid fishes [23], citrate synthase from an Antarctic bacteria [24], phosphoglycerate kinase from Antarctic Pseudomonas sp. TACII18 [25], anionic trypsin from Chum salmon (Oncorhynvhus keta) [26] and alkaline phosphatase from Atlantic cod (Gadus morhua) [27]. These findings suggest local flexibility as a strategy for cold adaptation.…”

Section: Introductionmentioning

confidence: 93%